ID   EFM7_CRYNJ              Reviewed;         299 AA.
AC   P0CP44; Q55PK4; Q5KDV2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Protein N-terminal and lysine N-methyltransferase EFM7 {ECO:0000255|HAMAP-Rule:MF_03223};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03223};
DE   AltName: Full=Elongation factor methyltransferase 7 {ECO:0000255|HAMAP-Rule:MF_03223};
GN   Name=EFM7 {ECO:0000255|HAMAP-Rule:MF_03223}; Synonyms=NNT1;
GN   OrderedLocusNames=CNG02680;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein methyltransferase
CC       that trimethylates the N-terminal glycine 'Gly-2' of elongation factor
CC       1-alpha, before also catalyzing the mono- and dimethylation of 'Lys-3'.
CC       {ECO:0000255|HAMAP-Rule:MF_03223}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03223}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. EFM7 family. {ECO:0000255|HAMAP-Rule:MF_03223}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW44624.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AE017347; AAW44624.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_571931.1; XM_571931.1.
DR   AlphaFoldDB; P0CP44; -.
DR   SMR; P0CP44; -.
DR   STRING; 5207.AAW44624; -.
DR   PaxDb; P0CP44; -.
DR   eggNOG; KOG2920; Eukaryota.
DR   InParanoid; P0CP44; -.
DR   OrthoDB; 1588190at2759; -.
DR   Proteomes; UP000002149; Chromosome 7.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0018013; P:N-terminal peptidyl-glycine methylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IBA:GO_Central.
DR   GO; GO:0000183; P:rDNA heterochromatin assembly; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_03223; Methyltr_EFM7; 1.
DR   InterPro; IPR025784; EFM7.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14614; PTHR14614; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51560; SAM_MT_NNT1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..299
FT                   /note="Protein N-terminal and lysine N-methyltransferase
FT                   EFM7"
FT                   /id="PRO_0000096893"
FT   BINDING         74
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT   BINDING         100..102
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT   BINDING         122
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT   BINDING         155
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT   BINDING         178
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
SQ   SEQUENCE   299 AA;  33358 MW;  6727D5648AF256EA CRC64;
     MSQDPILTSK GSQEEEDFFG LDNFFPEPES PLPPPFSFAS YDIPANIDFY VPDHRKSLIL
     RLVGSHPLWG HHLWNTARTL STYLLETPQI TQSRHVLELG AGAGLPSIVC VLAGSSKVIV
     TDYSDEGLLD NLRFNVDVNL EGEEKERIAV DGHVWGQSVD PLLGHLPKGQ KYDLLILSDL
     VFNHSQHDAL IKTVEATLTS SSTQSYDPSN PSAPLTEPSI LVFFTHHRPH LAHADMAFFP
     RLAESGNGWA YEKVVEEWAG AMFENDPGDK KVRGTVHGWR AWRVRDGEER GEKPSRISL